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Conserved domains on  [gi|76253908|ref|NP_998277|]
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geranylgeranyl transferase type-2 subunit beta [Danio rerio]

Protein Classification

geranylgeranyl transferase type-2 subunit beta( domain architecture ID 10121021)

geranylgeranyl transferase type-2 subunit beta is part of the catalytic component of the enzyme that catalyzes the transfer of a geranylgeranyl moiety from geranylgeranyl diphosphate to both cysteines of Rab proteins with the C-terminal sequence -XXCC, -XCXC and -CCXX, such as RAB1A, RAB3A, RAB5A and RAB7A

CATH:  1.50.10.20
EC:  2.5.1.60
Gene Ontology:  GO:0004663|GO:0018344|GO:0005968|GO:0031267|GO:0008270
PubMed:  8621375
SCOP:  4001193

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GGTase-II cd02894
Geranylgeranyltransferase type II (GGTase-II)_like proteins containing the protein ...
 18-301 0e+00

Geranylgeranyltransferase type II (GGTase-II)_like proteins containing the protein prenyltransferase (PTase) domain, beta subunit (alpha 6 - alpha 6 barrel fold). GGTase-IIs are a subgroup of the protein prenyltransferase family of lipid-modifying enzymes. PTases catalyze the carboxyl-terminal lipidation of Ras, Rab, and several other cellular signal transduction proteins, facilitating membrane associations and specific protein-protein interactions. Prenyltransferases employ a Zn2+ ion to alkylate a thiol group catalyzing the formation of thioether linkages between cysteine residues at or near the C-terminus of protein acceptors and the C1 atom of isoprenoid lipids (geranylgeranyl (20-carbon) in the case of GGTase-II ). GGTase-II catalyzes alkylation of both cysteine residues in Rab proteins containing carboxy-terminal "CC", "CXCX" or "CXC" motifs. PTases are heterodimeric with both alpha and beta subunits required for catalytic activity. In contrast to other prenyltransferases, GGTas-II requires an escort protein to bring the substrate protein to the catalytic heterodimer and to escort the geryanylgeranylated product to the membrane.


:

Pssm-ID: 239224 [Multi-domain]  Cd Length: 287  Bit Score: 544.94  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76253908  18 LFLDKHADYIAAYGSKKDDYEYTLSEYLRMSGIYWGLTVMDLMGQLSRMNREEIIEFIKSCQ-HDCGGISASIGHDPHLL 96
Cdd:cd02894   1 LLLEKHIEYILSLTKKKDDYEYILTEHLRMSGIYWGLTALDLLGQLERLNREEIIEFVKSCQdNEDGGFGGSPGHDPHIL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76253908  97 YTLSAIQILSLYDSVNAID--VDKVVEYVKGLQQEDGSFAGDKWGEIDTRFSFCAVATLALLGKLDVINVDKAVEFVMSC 174
Cdd:cd02894  81 STLSAIQILALYDLLNKIDenKEKIAKFIKGLQNEDGSFSGDKWGEVDTRFSYCAVLCLTLLGKLDLIDVDKAVDYLLSC 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76253908 175 MNFDGGFGCRPGSESHAGQIYCCTGFLSVTGQLHQVNADLLGWWLCERQLPSGGLNGRPEKLPDVCYSWWVLASLKIIGR 254
Cdd:cd02894 161 YNFDGGFGCRPGAESHAGQIFCCVGALAILGSLDLIDRDRLGWWLCERQLPSGGLNGRPEKLPDVCYSWWVLSSLKIIGR 240

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 76253908 255 IHWIDKAKLRNFILACQDEETGGFADRPGDMVDPFHTLFGVAGLSLL 301
Cdd:cd02894 241 LHWINKNKLKNFILACQDEEDGGFADRPGNMVDVFHTFFGLAGLSLL 287
 
Name Accession Description Interval E-value
GGTase-II cd02894
Geranylgeranyltransferase type II (GGTase-II)_like proteins containing the protein ...
 18-301 0e+00

Geranylgeranyltransferase type II (GGTase-II)_like proteins containing the protein prenyltransferase (PTase) domain, beta subunit (alpha 6 - alpha 6 barrel fold). GGTase-IIs are a subgroup of the protein prenyltransferase family of lipid-modifying enzymes. PTases catalyze the carboxyl-terminal lipidation of Ras, Rab, and several other cellular signal transduction proteins, facilitating membrane associations and specific protein-protein interactions. Prenyltransferases employ a Zn2+ ion to alkylate a thiol group catalyzing the formation of thioether linkages between cysteine residues at or near the C-terminus of protein acceptors and the C1 atom of isoprenoid lipids (geranylgeranyl (20-carbon) in the case of GGTase-II ). GGTase-II catalyzes alkylation of both cysteine residues in Rab proteins containing carboxy-terminal "CC", "CXCX" or "CXC" motifs. PTases are heterodimeric with both alpha and beta subunits required for catalytic activity. In contrast to other prenyltransferases, GGTas-II requires an escort protein to bring the substrate protein to the catalytic heterodimer and to escort the geryanylgeranylated product to the membrane.


Pssm-ID: 239224 [Multi-domain]  Cd Length: 287  Bit Score: 544.94  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76253908  18 LFLDKHADYIAAYGSKKDDYEYTLSEYLRMSGIYWGLTVMDLMGQLSRMNREEIIEFIKSCQ-HDCGGISASIGHDPHLL 96
Cdd:cd02894   1 LLLEKHIEYILSLTKKKDDYEYILTEHLRMSGIYWGLTALDLLGQLERLNREEIIEFVKSCQdNEDGGFGGSPGHDPHIL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76253908  97 YTLSAIQILSLYDSVNAID--VDKVVEYVKGLQQEDGSFAGDKWGEIDTRFSFCAVATLALLGKLDVINVDKAVEFVMSC 174
Cdd:cd02894  81 STLSAIQILALYDLLNKIDenKEKIAKFIKGLQNEDGSFSGDKWGEVDTRFSYCAVLCLTLLGKLDLIDVDKAVDYLLSC 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76253908 175 MNFDGGFGCRPGSESHAGQIYCCTGFLSVTGQLHQVNADLLGWWLCERQLPSGGLNGRPEKLPDVCYSWWVLASLKIIGR 254
Cdd:cd02894 161 YNFDGGFGCRPGAESHAGQIFCCVGALAILGSLDLIDRDRLGWWLCERQLPSGGLNGRPEKLPDVCYSWWVLSSLKIIGR 240

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 76253908 255 IHWIDKAKLRNFILACQDEETGGFADRPGDMVDPFHTLFGVAGLSLL 301
Cdd:cd02894 241 LHWINKNKLKNFILACQDEEDGGFADRPGNMVDVFHTFFGLAGLSLL 287
PLN03201 PLN03201
RAB geranylgeranyl transferase beta-subunit; Provisional
 14-326 0e+00

RAB geranylgeranyl transferase beta-subunit; Provisional


Pssm-ID: 215630 [Multi-domain]  Cd Length: 316  Bit Score: 517.71  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76253908   14 APNTLFLDKHADYIAAYGSKKDDYEYTLSEYLRMSGIYWGLTVMDLMGQLSRMNREEIIEFIKSCQHDCGGISASIGHDP 93
Cdd:PLN03201   4 PMGELVVDKHVRYIKSLEKKKDSFESVVMEHLRMNGAYWGLTALDLLGKLDDVDRDEVVSWVMRCQHESGGFGGNTGHDP 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76253908   94 HLLYTLSAIQILSLYDSVNAIDVDKVVEYVKGLQQEDGSFAGDKWGEIDTRFSFCAVATLALLGKLDVINVDKAVEFVMS 173
Cdd:PLN03201  84 HILYTLSAVQILALFDRLDLLDADKVASYVAGLQNEDGSFSGDEWGEIDTRFSYCALCCLSLLKRLDKINVEKAVDYIVS 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76253908  174 CMNFDGGFGCRPGSESHAGQIYCCTGFLSVTGQLHQVNADLLGWWLCERQLPSGGLNGRPEKLPDVCYSWWVLASLKIIG 253
Cdd:PLN03201 164 CKNFDGGFGCTPGGESHAGQIFCCVGALAITGSLHHVDKDLLGWWLCERQVKSGGLNGRPEKLPDVCYSWWVLSSLIIID 243

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 76253908  254 RIHWIDKAKLRNFILACQDEETGGFADRPGDMVDPFHTLFGVAGLSLLGDEQIKPVNPVFCMPEDVLQRIGLQ 326
Cdd:PLN03201 244 RVHWIDKDKLAKFILDCQDDENGGISDRPDDAVDVFHTFFGVAGLSLLGYPGLKPIDPAYALPVDVVNRIGLR 316
CAL1 COG5029
Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, ...
 68-302 1.84e-29

Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, Lipid transport and metabolism];


Pssm-ID: 444045 [Multi-domain]  Cd Length: 259  Bit Score: 113.26  E-value: 1.84e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76253908  68 REEIIEFIKSCQHDCGGISASIGhDPHLLYTLSAIQILSLYDSVNAIDvDKVVEYVKGLQQEDGSFA-GDKWGEIDTRFS 146
Cdd:COG5029  21 TDSHLDYLRASQNPDGGFAGRSG-PSDLYSTYYAVRTLALLGESPKWR-DRVADLLSSLRVEDGGFAkAPEGGAGSTYHT 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76253908 147 FCAVATLALLGkLDVINVDKAVEFVMSCMNFDGGFGCRPGSESHAGQIYCCTGFLSVTGQLHQVNADLLGWWLCERQLPS 226
Cdd:COG5029  99 YLATLLAELLG-RPPPDPDRLVRFLISQQNDDGGFEISPGRRSDTNPTAAAIGALRALGALDDPIETKVIRFLRDVQSPE 177

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 76253908 227 GGLNGRPEK-LPDVCYSWWVLASLKIIGrIHWIDKAKLRNFILACQDEEtGGFADRPGDMV-DPFHTLFGVAGLSLLG 302
Cdd:COG5029 178 GGFAYNTRIgEADLLSTFTAILTLYDLG-AAPKLVDDLQAYILSLQLPD-GGFEGAPWDGVeDVEYTFYGVGALALLG 253
Prenyltrans pfam00432
Prenyltransferase and squalene oxidase repeat;
114-157 1.83e-12

Prenyltransferase and squalene oxidase repeat;


Pssm-ID: 395346 [Multi-domain]  Cd Length: 44  Bit Score: 60.99  E-value: 1.83e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 76253908   114 IDVDKVVEYVKGLQQEDGSFAGDKWGEIDTRFSFCAVATLALLG 157
Cdd:pfam00432   1 IDKEKLVDYLLSCQNEDGGFGGRPGGESDTYYTYCALAALALLG 44
squalene_cyclas TIGR01787
squalene/oxidosqualene cyclases; This family of enzymes catalyzes the cyclization of the ...
 98-182 6.95e-05

squalene/oxidosqualene cyclases; This family of enzymes catalyzes the cyclization of the triterpenes squalene or 2-3-oxidosqualene to a variety of products including hopene, lanosterol, cycloartenol, amyrin, lupeol, and isomultiflorenol.


Pssm-ID: 273809 [Multi-domain]  Cd Length: 621  Bit Score: 44.35  E-value: 6.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76253908    98 TLSAIQILSLYDSvNAIDVDKV----VEYVKGLQQEDGSFAGdKWGEIDTRFSFCAVATLALLGKL--DVINVDKAVEFV 171
Cdd:TIGR01787 441 TARVIQALGAFGH-RADEIRNVleraLEYLRREQRADGSWFG-RWGVNYTYGTGFVLSALAAAGRTyrNCPEVQKACDWL 518

                          90
                  ....*....|.
gi 76253908   172 MSCMNFDGGFG 182
Cdd:TIGR01787 519 LSRQMPDGGWG 529
 
Name Accession Description Interval E-value
GGTase-II cd02894
Geranylgeranyltransferase type II (GGTase-II)_like proteins containing the protein ...
 18-301 0e+00

Geranylgeranyltransferase type II (GGTase-II)_like proteins containing the protein prenyltransferase (PTase) domain, beta subunit (alpha 6 - alpha 6 barrel fold). GGTase-IIs are a subgroup of the protein prenyltransferase family of lipid-modifying enzymes. PTases catalyze the carboxyl-terminal lipidation of Ras, Rab, and several other cellular signal transduction proteins, facilitating membrane associations and specific protein-protein interactions. Prenyltransferases employ a Zn2+ ion to alkylate a thiol group catalyzing the formation of thioether linkages between cysteine residues at or near the C-terminus of protein acceptors and the C1 atom of isoprenoid lipids (geranylgeranyl (20-carbon) in the case of GGTase-II ). GGTase-II catalyzes alkylation of both cysteine residues in Rab proteins containing carboxy-terminal "CC", "CXCX" or "CXC" motifs. PTases are heterodimeric with both alpha and beta subunits required for catalytic activity. In contrast to other prenyltransferases, GGTas-II requires an escort protein to bring the substrate protein to the catalytic heterodimer and to escort the geryanylgeranylated product to the membrane.


Pssm-ID: 239224 [Multi-domain]  Cd Length: 287  Bit Score: 544.94  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76253908  18 LFLDKHADYIAAYGSKKDDYEYTLSEYLRMSGIYWGLTVMDLMGQLSRMNREEIIEFIKSCQ-HDCGGISASIGHDPHLL 96
Cdd:cd02894   1 LLLEKHIEYILSLTKKKDDYEYILTEHLRMSGIYWGLTALDLLGQLERLNREEIIEFVKSCQdNEDGGFGGSPGHDPHIL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76253908  97 YTLSAIQILSLYDSVNAID--VDKVVEYVKGLQQEDGSFAGDKWGEIDTRFSFCAVATLALLGKLDVINVDKAVEFVMSC 174
Cdd:cd02894  81 STLSAIQILALYDLLNKIDenKEKIAKFIKGLQNEDGSFSGDKWGEVDTRFSYCAVLCLTLLGKLDLIDVDKAVDYLLSC 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76253908 175 MNFDGGFGCRPGSESHAGQIYCCTGFLSVTGQLHQVNADLLGWWLCERQLPSGGLNGRPEKLPDVCYSWWVLASLKIIGR 254
Cdd:cd02894 161 YNFDGGFGCRPGAESHAGQIFCCVGALAILGSLDLIDRDRLGWWLCERQLPSGGLNGRPEKLPDVCYSWWVLSSLKIIGR 240

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 76253908 255 IHWIDKAKLRNFILACQDEETGGFADRPGDMVDPFHTLFGVAGLSLL 301
Cdd:cd02894 241 LHWINKNKLKNFILACQDEEDGGFADRPGNMVDVFHTFFGLAGLSLL 287
PLN03201 PLN03201
RAB geranylgeranyl transferase beta-subunit; Provisional
 14-326 0e+00

RAB geranylgeranyl transferase beta-subunit; Provisional


Pssm-ID: 215630 [Multi-domain]  Cd Length: 316  Bit Score: 517.71  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76253908   14 APNTLFLDKHADYIAAYGSKKDDYEYTLSEYLRMSGIYWGLTVMDLMGQLSRMNREEIIEFIKSCQHDCGGISASIGHDP 93
Cdd:PLN03201   4 PMGELVVDKHVRYIKSLEKKKDSFESVVMEHLRMNGAYWGLTALDLLGKLDDVDRDEVVSWVMRCQHESGGFGGNTGHDP 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76253908   94 HLLYTLSAIQILSLYDSVNAIDVDKVVEYVKGLQQEDGSFAGDKWGEIDTRFSFCAVATLALLGKLDVINVDKAVEFVMS 173
Cdd:PLN03201  84 HILYTLSAVQILALFDRLDLLDADKVASYVAGLQNEDGSFSGDEWGEIDTRFSYCALCCLSLLKRLDKINVEKAVDYIVS 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76253908  174 CMNFDGGFGCRPGSESHAGQIYCCTGFLSVTGQLHQVNADLLGWWLCERQLPSGGLNGRPEKLPDVCYSWWVLASLKIIG 253
Cdd:PLN03201 164 CKNFDGGFGCTPGGESHAGQIFCCVGALAITGSLHHVDKDLLGWWLCERQVKSGGLNGRPEKLPDVCYSWWVLSSLIIID 243

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 76253908  254 RIHWIDKAKLRNFILACQDEETGGFADRPGDMVDPFHTLFGVAGLSLLGDEQIKPVNPVFCMPEDVLQRIGLQ 326
Cdd:PLN03201 244 RVHWIDKDKLAKFILDCQDDENGGISDRPDDAVDVFHTFFGVAGLSLLGYPGLKPIDPAYALPVDVVNRIGLR 316
PTase cd02890
Protein prenyltransferase (PTase) domain, beta subunit (alpha 6 - alpha 6 barrel fold). The ...
 20-301 4.51e-149

Protein prenyltransferase (PTase) domain, beta subunit (alpha 6 - alpha 6 barrel fold). The protein prenyltransferase family of lipid-modifying enzymes includes protein farnesyltransferase (FTase) and geranylgeranyltransferase types I and II (GGTase-I and GGTase-II). They catalyze the carboxyl-terminal lipidation of Ras, Rab, and several other cellular signal transduction proteins, facilitating membrane associations and specific protein-protein interactions. Prenyltransferases employ a Zn2+ ion to alkylate a thiol group catalyzing the formation of thioether linkages between the C1 atom of farnesyl (15-carbon by FTase) or geranylgeranyl (20-carbon by GGTase-I, II) isoprenoid lipids and cysteine residues at or near the C-terminus of protein acceptors. FTase and GGTase-I prenylate the cysteine in the terminal sequence, "CAAX"; and GGTase-II prenylates both cysteines in the "CC" (or "CXC") terminal sequence. These enzymes are heterodimeric with both alpha and beta subunits required for catalytic activity. In contrast to other prenyltransferases, GGTase-II does not recognize its protein acceptor directly but requires Rab to complex with REP (Rab escort protein) before prenylation can occur. These enzymes are found exclusively in eukaryotes.


Pssm-ID: 239220 [Multi-domain]  Cd Length: 286  Bit Score: 420.45  E-value: 4.51e-149
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76253908  20 LDKHADYIAAYGsKKDDYEYTLSEYLRMSGIYWGLTVMDLMGQ-LSRMNREEIIEFIKSCQ-HDCGGISASIGHDPHLLY 97
Cdd:cd02890   1 REKHIKYLQRCL-KLLPSSYTSLDASRLWLLYWILSSLDLLGEdLDDENKDEIIDFIYSCQvNEDGGFGGGPGQDPHLAS 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76253908  98 TLSAIQILSLYDS--VNAIDVDKVVEYVKGLQQEDGSFAGDKWGEIDTRFSFCAVATLALLGKLDVINVDKAVEFVMSCM 175
Cdd:cd02890  80 TYAAVLSLAILGDdaLSRIDREKIYKFLSSLQNPDGSFRGDLGGEVDTRFVYCALSILSLLNILTDIDKEKLIDYILSCQ 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76253908 176 NFDGGFGCRPGSESHAGQIYCCTGFLSVTGQLHQVNADLLGWWLCERQLPSG-GLNGRPEKLPDVCYSWWVLASLKIIGR 254
Cdd:cd02890 160 NYDGGFGGVPGAESHGGYTFCAVASLALLGRLDLIDKERLLRWLVERQLASGgGFNGRPNKLVDTCYSFWVGASLKILGR 239

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 76253908 255 IHWIDKAKLRNFILACQDEETGGFADRPGDMVDPFHTLFGVAGLSLL 301
Cdd:cd02890 240 LHLIDQEKLREYILSCQQSEVGGFSDKPGKPPDLYHTYYGLSGLSLL 286
ISOPREN_C2_like cd00688
This group contains class II terpene cyclases, protein prenyltransferases beta subunit, two ...
 20-301 4.05e-78

This group contains class II terpene cyclases, protein prenyltransferases beta subunit, two broadly specific proteinase inhibitors alpha2-macroglobulin (alpha (2)-M) and pregnancy zone protein (PZP) and, the C3 C4 and C5 components of vertebrate complement. Class II terpene cyclases include squalene cyclase (SQCY) and 2,3-oxidosqualene cyclase (OSQCY), these integral membrane proteins catalyze a cationic cyclization cascade converting linear triterpenes to fused ring compounds. The protein prenyltransferases include protein farnesyltransferase (FTase) and geranylgeranyltransferase types I and II (GGTase-I and GGTase-II) which catalyze the carboxyl-terminal lipidation of Ras, Rab, and several other cellular signal transduction proteins, facilitating membrane associations and specific protein-protein interactions. Alpha (2)-M is a major carrier protein in serum and involved in the immobilization and entrapment of proteases. PZP is a pregnancy associated protein. Alpha (2)-M and PZP are known to bind to and, may modulate, the activity of placental protein-14 in T-cell growth and cytokine production thereby protecting the allogeneic fetus from attack by the maternal immune system.


Pssm-ID: 238362 [Multi-domain]  Cd Length: 300  Bit Score: 240.92  E-value: 4.05e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76253908  20 LDKHADYIAAYGsKKDDYEYTLSEYLRMSGIYWGLTVMDLMGQLS------RMNREEIIEFIKSCQHDCGGISASIGHD- 92
Cdd:cd00688   1 IEKHLKYLLRYP-YGDGHWYQSLCGEQTWSTAWPLLALLLLLAATgirdkaDENIEKGIQRLLSYQLSDGGFSGWGGNDy 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76253908  93 PHLLYTLSAIQILSL---YDSVNAIDVDKVVEYVKGLQQEDGSFAGDKWG-------EIDTRFSFCAVATLALLGKLDV- 161
Cdd:cd00688  80 PSLWLTAYALKALLLagdYIAVDRIDLARALNWLLSLQNEDGGFREDGPGnhriggdESDVRLTAYALIALALLGKLDPd 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76253908 162 INVDKAVEFVMSCMNFDGGFGcrPGSESHAGQIYCCTGFLSVTGQLHQVNADLLGWWLCERQLPSGGLNGRPE---KLPD 238
Cdd:cd00688 160 PLIEKALDYLLSCQNYDGGFG--PGGESHGYGTACAAAALALLGDLDSPDAKKALRWLLSRQRPDGGWGEGRDrtnKLSD 237

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 76253908 239 VCYSWWVLASLKIIGRI-HWIDKAKLRNFILACQDeETGGFADRPGDMVDPFHTLFGVAGLSLL 301
Cdd:cd00688 238 SCYTEWAAYALLALGKLgDLEDAEKLVKWLLSQQN-EDGGFSSKPGKSYDTQHTVFALLALSLY 300
GGTase-I cd02895
Geranylgeranyltransferase types I (GGTase-I)-like proteins containing the protein ...
 46-301 7.66e-72

Geranylgeranyltransferase types I (GGTase-I)-like proteins containing the protein prenyltransferase (PTase) domain, beta subunit (alpha 6 - alpha 6 barrel fold). GGTase-I s are a subgroup of the protein prenyltransferase family of lipid-modifying enzymes PTases catalyze the carboxyl-terminal lipidation of Ras, Rab, and several other cellular signal transduction proteins, facilitating membrane associations and specific protein-protein interactions. Prenyltransferases employ a Zn2+ ion to alkylate a thiol group catalyzing the formation of thioether linkages between cysteine residues at or near the C-terminus of protein acceptors and the C1 atom of isoprenoid lipids (geranylgeranyl (20-carbon) in the case of GGTase-I ). GGTase-I prenylates the cysteine in the terminal sequence, "CAAX" when X is Leu or Phe. Substrates for GTTase-I include the gamma subunit of neural G-proteins and several Ras-related G-proteins. PTases are heterodimeric with both alpha and beta subunits required for catalytic activity.


Pssm-ID: 239225 [Multi-domain]  Cd Length: 307  Bit Score: 224.85  E-value: 7.66e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76253908  46 RMSGIYWGLTVMDLMGQL---SRMNREEIIEFIKSCQ----HDCGGISASIGHD----------PHLLYTLSAIQILS-L 107
Cdd:cd02895  26 RLTIAFFALSGLDLLGALdsiLVEEKDDIIEWIYSLQvlsnLPRGGFRGSSTLGlpgtaskydtGNLAMTYFALLSLLiL 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76253908 108 YDSVNAIDVDKVVEYVKGLQQEDGSFAGDKW---GEIDTRFSFCAVATLALLG--KLDVINVDKAVEFVMSCMNFDGGFG 182
Cdd:cd02895 106 GDDLSRVDRKAILNFLSKLQLPDGSFGSVLDsegGENDMRFCYCAVAICYMLDdwSEEDIDKEKLIDYIKSSQSYDGGFG 185

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76253908 183 CRPGSESHAGQIYCCTGFLSVTGQLHQVNADLLGW---WLCERQLPSGGLNGRPEKLPDVCYSWWVLASLKIIGRIHWID 259
Cdd:cd02895 186 QGPGLESHGGSTFCAIASLSLLGKLEELSEKFLERlkrWLVHRQVSGTGFNGRPNKPADTCYSFWVGASLKLLDAFQLID 265

                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 76253908 260 KAKLRNFILACQDEETGGFADRPGDMVDPFHTLFGVAGLSLL 301
Cdd:cd02895 266 FEKNRNYLLSTQQSLVGGFAKNPDSHPDPLHSYLGLAALSLI 307
FTase cd02893
Protein farnesyltransferase (FTase)_like proteins containing the protein prenyltransferase ...
 50-300 1.62e-62

Protein farnesyltransferase (FTase)_like proteins containing the protein prenyltransferase (PTase) domain, beta subunit (alpha 6 - alpha 6 barrel fold). FTases are a subgroup of PTase family of lipid-modifying enzymes. PTases catalyze the carboxyl-terminal lipidation of Ras, Rab, and several other cellular signal transduction proteins, facilitating membrane associations and specific protein-protein interactions. These proteins are heterodimers of alpha and beta subunits. Both subunits are required for catalytic activity. Prenyltransferases employ a Zn2+ ion to alkylate a thiol group catalyzing the formation of thioether linkages between cysteine residues at or near the C-terminus of protein acceptors and the C1 atom of isoprenoid lipids. Ftase attaches a 15-carbon farnesyl group to the cysteine within the C-terminal CaaX motif of substrate proteins when X is Ala, Met, Ser, Cys or Gln. Protein farnesylation has been shown to play critical roles in a variety of cellular processes including Ras/mitogen activated protein kinase signaling pathways in mammals and, abscisic acid signal transduction in Arabidopsis.


Pssm-ID: 239223 [Multi-domain]  Cd Length: 299  Bit Score: 200.92  E-value: 1.62e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76253908  50 IYWGLTVMDLMG-QLSRMNREEIIEFIKSCQHDCGGISASIGHDPHLLYTLSAIQILSLYDSVNA---IDVDKVVEYVKG 125
Cdd:cd02893  30 LYWILHSLELLGeELDQSYADDVISFLRRCQNPSGGFGGGPGQLPHLATTYAAVNALAIIGTEEAydvIDREALYKFLLS 109

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76253908 126 LQQEDGSFAGDKWGEIDTRFSFCAVATLALLGKLDVINVDKAVEFVMSCMNFDGGFGCRPGSESHAGQIYCCTGFLSVTG 205
Cdd:cd02893 110 LKQPDGSFRMHVGGEVDVRGTYCAISVASLLNILTDELFEGVAEYILSCQTYEGGFGGVPGNEAHGGYTFCALAALAILG 189

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76253908 206 QLHQVNADLLGWWLCERQLPS-GGLNGRPEKLPDVCYSWWVLASLKIIGRI------------HW-IDKAKLRNFILACQ 271
Cdd:cd02893 190 KPDKLDLESLLRWLVARQMRFeGGFQGRTNKLVDGCYSFWVGGSLPILEAIlnaekkfddsaeGTlFDQEALQEYILLCC 269

                       250       260
                ....*....|....*....|....*....
gi 76253908 272 DEETGGFADRPGDMVDPFHTLFGVAGLSL 300
Cdd:cd02893 270 QSEEGGLRDKPGKPRDFYHTCYALSGLSI 298
PLN02710 PLN02710
farnesyltranstransferase subunit beta
 18-299 2.92e-31

farnesyltranstransferase subunit beta


Pssm-ID: 215380 [Multi-domain]  Cd Length: 439  Bit Score: 121.82  E-value: 2.92e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76253908   18 LFLDKHADYIAAyGSKKDDYEYTLSEYLRMSGIYWGLTVMDLMGQLSRMNRE-EIIEFIKSCQHDCGGISASIGHDPHLL 96
Cdd:PLN02710  44 LWREKHLEYLTR-GLRQLGPSFSVLDANRPWLCYWILHSIALLGESLDDELEnDTIDFLSRCQDPNGGYGGGPGQLPHLA 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76253908   97 YTLSAIQILSLYDSVNA---IDVDKVVEYVKGLQQEDGSFAGDKWGEIDTRFSFCAVATLALLGKLDVINVDKAVEFVMS 173
Cdd:PLN02710 123 TTYAAVNTLVTIGGERAlssINREKLYTFLLRMKDPSGGFRMHDGGEMDVRACYTAISVASLLNILDDELVKGVGDYILS 202

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76253908  174 CMNFDGGFGCRPGSESHAGQIYCCTGFLSVTGQLHQVNADLLGWWLCERQLPSGGLNGRPEKLPDVCYSWWVLASLKIIG 253
Cdd:PLN02710 203 CQTYEGGIGGEPGAEAHGGYTFCGLAAMILINEVDRLDLPSLINWVVFRQGVEGGFQGRTNKLVDGCYSFWQGGVFALLQ 282

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76253908  254 RIHWIDKAK-----------------------------------------------------------LRNFILACQDEE 274
Cdd:PLN02710 283 QLVTIVDEQlqtggssimfeeleddacetsssgkddagdtdsadyskvgfdfikasnqqmgplfhsiaLQQYILLCSQVL 362

                        330       340
                 ....*....|....*....|....*
gi 76253908  275 TGGFADRPGDMVDPFHTLFGVAGLS 299
Cdd:PLN02710 363 DGGLRDKPGKSRDYYHTCYCLSGLS 387
CAL1 COG5029
Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, ...
 68-302 1.84e-29

Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, Lipid transport and metabolism];


Pssm-ID: 444045 [Multi-domain]  Cd Length: 259  Bit Score: 113.26  E-value: 1.84e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76253908  68 REEIIEFIKSCQHDCGGISASIGhDPHLLYTLSAIQILSLYDSVNAIDvDKVVEYVKGLQQEDGSFA-GDKWGEIDTRFS 146
Cdd:COG5029  21 TDSHLDYLRASQNPDGGFAGRSG-PSDLYSTYYAVRTLALLGESPKWR-DRVADLLSSLRVEDGGFAkAPEGGAGSTYHT 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76253908 147 FCAVATLALLGkLDVINVDKAVEFVMSCMNFDGGFGCRPGSESHAGQIYCCTGFLSVTGQLHQVNADLLGWWLCERQLPS 226
Cdd:COG5029  99 YLATLLAELLG-RPPPDPDRLVRFLISQQNDDGGFEISPGRRSDTNPTAAAIGALRALGALDDPIETKVIRFLRDVQSPE 177

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 76253908 227 GGLNGRPEK-LPDVCYSWWVLASLKIIGrIHWIDKAKLRNFILACQDEEtGGFADRPGDMV-DPFHTLFGVAGLSLLG 302
Cdd:COG5029 178 GGFAYNTRIgEADLLSTFTAILTLYDLG-AAPKLVDDLQAYILSLQLPD-GGFEGAPWDGVeDVEYTFYGVGALALLG 253
CAL1 COG5029
Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, ...
 14-254 1.72e-21

Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, Lipid transport and metabolism];


Pssm-ID: 444045 [Multi-domain]  Cd Length: 259  Bit Score: 91.69  E-value: 1.72e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76253908  14 APNTLFLDKHADYIAA-------YG--SKKDDYEYTlseylrmsgiYWGLTVMDLMGQLSRmNREEIIEFIKSCQ-HDCG 83
Cdd:COG5029  15 KSTADFTDSHLDYLRAsqnpdggFAgrSGPSDLYST----------YYAVRTLALLGESPK-WRDRVADLLSSLRvEDGG 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76253908  84 GISASIGHDPHLLYTLSAIQILSLYD-SVNaiDVDKVVEYVKGLQQEDGSFAGDKWGEIDTRFSFCAVATLALLGKLDVI 162
Cdd:COG5029  84 FAKAPEGGAGSTYHTYLATLLAELLGrPPP--DPDRLVRFLISQQNDDGGFEISPGRRSDTNPTAAAIGALRALGALDDP 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76253908 163 NVDKAVEFVMSCMNFDGGFGCRPgSESHAGQIYCCTGFLSvtgqLHQVNA-----DLLGWWLCERQLPSGGLNGRP-EKL 236
Cdd:COG5029 162 IETKVIRFLRDVQSPEGGFAYNT-RIGEADLLSTFTAILT----LYDLGAapklvDDLQAYILSLQLPDGGFEGAPwDGV 236

                       250
                ....*....|....*...
gi 76253908 237 PDVCYSWWVLASLKIIGR 254
Cdd:COG5029 237 EDVEYTFYGVGALALLGA 254
AF1543 COG1689
Class II terpene cyclase family protein AF1543 [General function prediction only];
64-302 8.78e-19

Class II terpene cyclase family protein AF1543 [General function prediction only];


Pssm-ID: 441295 [Multi-domain]  Cd Length: 272  Bit Score: 84.39  E-value: 8.78e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76253908  64 SRMNREEIIEFIKSCQHDCGGISASIGHDPHLLYTLSAIQILSLYDSVNAiDVDKVVEYVKGLQQEDGSFAGdkwgeidT 143
Cdd:COG1689   4 LRFDLARTIEYVLKRQNEDGGFCAYPGLPSTLADTYYAVRILKLLGEEVP-NRDKTIEFLESCQDEEGGGFA-------L 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76253908 144 RFSFCAVATLALLGKLDVINvDKAVEfvmscMNFDGGFGCRPGSESHAGQIYCCT-GFLSvtgqLHQVNADLLGW--WLC 220
Cdd:COG1689  76 YTTSYGLMALALLGIDPPDE-QEALE-----YLSDALPTKFAGGASDLEETYLAVaLLEA----LGASEPEREKIreFLL 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76253908 221 ERQLPSGGLNGrpeKLPDVCYSWWVLASLKIIGRiHWIDKAKLRNFILACQDeETGGFADRPGDMVDPFHTLFGVAGLSL 300
Cdd:COG1689 146 SLRRPDGGFGG---KKPNLEDTYWALAALRRLGR-DLPPADRVIAFILACQN-EDGGFSKTPGSYSDLEATYYALRALKL 220


                ..
gi 76253908 301 LG 302
Cdd:COG1689 221 LG 222
AF1543 COG1689
Class II terpene cyclase family protein AF1543 [General function prediction only];
50-185 5.81e-15

Class II terpene cyclase family protein AF1543 [General function prediction only];


Pssm-ID: 441295 [Multi-domain]  Cd Length: 272  Bit Score: 73.61  E-value: 5.81e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76253908  50 IYWGLTVMDLMGQLSRMnREEIIEFIKSCQHDCGGISASighDPHLLYTLSAIQILSL--YDSVNAidvDKVVEYVKGLQ 127
Cdd:COG1689 120 TYLAVALLEALGASEPE-REKIREFLLSLRRPDGGFGGK---KPNLEDTYWALAALRRlgRDLPPA---DRVIAFILACQ 192

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 76253908 128 QEDGSFA---GDKWgeiDTRFSFCAVATLALLGKlDVINVDKAVEFVMSCMNFDGGFGCRP 185
Cdd:COG1689 193 NEDGGFSktpGSYS---DLEATYYALRALKLLGE-PPKNVDKLLEFIASCQNSDGGFRRSP 249
Prenyltrans pfam00432
Prenyltransferase and squalene oxidase repeat;
114-157 1.83e-12

Prenyltransferase and squalene oxidase repeat;


Pssm-ID: 395346 [Multi-domain]  Cd Length: 44  Bit Score: 60.99  E-value: 1.83e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 76253908   114 IDVDKVVEYVKGLQQEDGSFAGDKWGEIDTRFSFCAVATLALLG 157
Cdd:pfam00432   1 IDKEKLVDYLLSCQNEDGGFGGRPGGESDTYYTYCALAALALLG 44
Prenyltrans pfam00432
Prenyltransferase and squalene oxidase repeat;
210-253 2.19e-11

Prenyltransferase and squalene oxidase repeat;


Pssm-ID: 395346 [Multi-domain]  Cd Length: 44  Bit Score: 57.91  E-value: 2.19e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 76253908   210 VNADLLGWWLCERQLPSGGLNGRPEKLPDVCYSWWVLASLKIIG 253
Cdd:pfam00432   1 IDKEKLVDYLLSCQNEDGGFGGRPGGESDTYYTYCALAALALLG 44
Prenyltrans pfam00432
Prenyltransferase and squalene oxidase repeat;
162-205 2.21e-11

Prenyltransferase and squalene oxidase repeat;


Pssm-ID: 395346 [Multi-domain]  Cd Length: 44  Bit Score: 57.91  E-value: 2.21e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 76253908   162 INVDKAVEFVMSCMNFDGGFGCRPGSESHAGQIYCCTGFLSVTG 205
Cdd:pfam00432   1 IDKEKLVDYLLSCQNEDGGFGGRPGGESDTYYTYCALAALALLG 44
CAL1 COG5029
Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, ...
 165-303 8.21e-11

Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, Lipid transport and metabolism];


Pssm-ID: 444045 [Multi-domain]  Cd Length: 259  Bit Score: 61.65  E-value: 8.21e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76253908 165 DKAVEFVMSCMNFDGGFGCRPGsESHAGQIYCCTGFLSVTGQLHQVNADLLGWWL-CERqlPSGGLNGRPEKLPDVCY-S 242
Cdd:COG5029  22 DSHLDYLRASQNPDGGFAGRSG-PSDLYSTYYAVRTLALLGESPKWRDRVADLLSsLRV--EDGGFAKAPEGGAGSTYhT 98

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 76253908 243 WWVLASLKIIGRiHWIDKAKLRNFILACQDEEtGGFADRPGDMVDPFHTLFGVAGLSLLGD 303
Cdd:COG5029  99 YLATLLAELLGR-PPPDPDRLVRFLISQQNDD-GGFEISPGRRSDTNPTAAAIGALRALGA 157
Prenyltrans pfam00432
Prenyltransferase and squalene oxidase repeat;
258-302 1.15e-10

Prenyltransferase and squalene oxidase repeat;


Pssm-ID: 395346 [Multi-domain]  Cd Length: 44  Bit Score: 55.98  E-value: 1.15e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 76253908   258 IDKAKLRNFILACQDEEtGGFADRPGDMVDPFHTLFGVAGLSLLG 302
Cdd:pfam00432   1 IDKEKLVDYLLSCQNED-GGFGGRPGGESDTYYTYCALAALALLG 44
Prenyltrans pfam00432
Prenyltransferase and squalene oxidase repeat;
66-109 4.51e-10

Prenyltransferase and squalene oxidase repeat;


Pssm-ID: 395346 [Multi-domain]  Cd Length: 44  Bit Score: 54.44  E-value: 4.51e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 76253908    66 MNREEIIEFIKSCQHDCGGISASIGHDPHLLYTLSAIQILSLYD 109
Cdd:pfam00432   1 IDKEKLVDYLLSCQNEDGGFGGRPGGESDTYYTYCALAALALLG 44
CAL1 COG5029
Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, ...
 51-161 1.00e-07

Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, Lipid transport and metabolism];


Pssm-ID: 444045 [Multi-domain]  Cd Length: 259  Bit Score: 52.40  E-value: 1.00e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76253908  51 YWGLTVMDLMGQLSRMNREEIIEFIKSCQHDCGGISA--SIGhDPHLLYTLSAIQILSlYDSVNAIDVDKVVEYVKGLQQ 128
Cdd:COG5029 146 AAAIGALRALGALDDPIETKVIRFLRDVQSPEGGFAYntRIG-EADLLSTFTAILTLY-DLGAAPKLVDDLQAYILSLQL 223

                        90       100       110
                ....*....|....*....|....*....|....
gi 76253908 129 EDGSFAGDKWGEI-DTRFSFCAVATLALLGKLDV 161
Cdd:COG5029 224 PDGGFEGAPWDGVeDVEYTFYGVGALALLGALAE 257
PTase cd02890
Protein prenyltransferase (PTase) domain, beta subunit (alpha 6 - alpha 6 barrel fold). The ...
 220-310 2.43e-07

Protein prenyltransferase (PTase) domain, beta subunit (alpha 6 - alpha 6 barrel fold). The protein prenyltransferase family of lipid-modifying enzymes includes protein farnesyltransferase (FTase) and geranylgeranyltransferase types I and II (GGTase-I and GGTase-II). They catalyze the carboxyl-terminal lipidation of Ras, Rab, and several other cellular signal transduction proteins, facilitating membrane associations and specific protein-protein interactions. Prenyltransferases employ a Zn2+ ion to alkylate a thiol group catalyzing the formation of thioether linkages between the C1 atom of farnesyl (15-carbon by FTase) or geranylgeranyl (20-carbon by GGTase-I, II) isoprenoid lipids and cysteine residues at or near the C-terminus of protein acceptors. FTase and GGTase-I prenylate the cysteine in the terminal sequence, "CAAX"; and GGTase-II prenylates both cysteines in the "CC" (or "CXC") terminal sequence. These enzymes are heterodimeric with both alpha and beta subunits required for catalytic activity. In contrast to other prenyltransferases, GGTase-II does not recognize its protein acceptor directly but requires Rab to complex with REP (Rab escort protein) before prenylation can occur. These enzymes are found exclusively in eukaryotes.


Pssm-ID: 239220 [Multi-domain]  Cd Length: 286  Bit Score: 51.43  E-value: 2.43e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76253908 220 CERQLPSGGLNGRPEKLpdvCYSWWVLASLKIIGR-IHWIDKAKLRNFILACQDEETGGFADRPGDMVDPFHTLFGVAGL 298
Cdd:cd02890  11 CLKLLPSSYTSLDASRL---WLLYWILSSLDLLGEdLDDENKDEIIDFIYSCQVNEDGGFGGGPGQDPHLASTYAAVLSL 87

                        90
                ....*....|..
gi 76253908 299 SLLGDEQIKPVN 310
Cdd:cd02890  88 AILGDDALSRID 99
PLN02710 PLN02710
farnesyltranstransferase subunit beta
 117-303 4.21e-07

farnesyltranstransferase subunit beta


Pssm-ID: 215380 [Multi-domain]  Cd Length: 439  Bit Score: 51.32  E-value: 4.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76253908  117 DKVVEYV-KGLQQEDGSF----AGDKWgeidtrFSFCAVATLALLGK-LDVINVDKAVEFVMSCMNFDGGFGCRPGSESH 190
Cdd:PLN02710  47 EKHLEYLtRGLRQLGPSFsvldANRPW------LCYWILHSIALLGEsLDDELENDTIDFLSRCQDPNGGYGGGPGQLPH 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76253908  191 AGQIYCCTGFLSVTG---QLHQVNADLLGWWLCERQLPSGGLNGRPEKLPDV--CYSWWVLASLKIIGRIHWIDKakLRN 265
Cdd:PLN02710 121 LATTYAAVNTLVTIGgerALSSINREKLYTFLLRMKDPSGGFRMHDGGEMDVraCYTAISVASLLNILDDELVKG--VGD 198

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 76253908  266 FILACQDEEtGGFADRPGDMVDPFHTLFGVAGLSLLGD 303
Cdd:PLN02710 199 YILSCQTYE-GGIGGEPGAEAHGGYTFCGLAAMILINE 235
PLN03012 PLN03012
Camelliol C synthase
 98-182 5.19e-06

Camelliol C synthase


Pssm-ID: 166653 [Multi-domain]  Cd Length: 759  Bit Score: 48.09  E-value: 5.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76253908   98 TLSAIQILSLY---------DSVNAIdVDKVVEYVKGLQQEDGSFAGDkWGEIDTRFSFCAVATLALLGKL--DVINVDK 166
Cdd:PLN03012 566 TSSAIQALILFkqlypdhrtEEINAF-IKKAAEYIENIQMLDGSWYGN-WGICFTYGTWFALAGLAAAGKTfnDCEAIRK 643

                         90
                 ....*....|....*.
gi 76253908  167 AVEFVMSCMNFDGGFG 182
Cdd:PLN03012 644 GVHFLLAAQKDNGGWG 659
squalene_cyclas TIGR01787
squalene/oxidosqualene cyclases; This family of enzymes catalyzes the cyclization of the ...
 98-182 6.95e-05

squalene/oxidosqualene cyclases; This family of enzymes catalyzes the cyclization of the triterpenes squalene or 2-3-oxidosqualene to a variety of products including hopene, lanosterol, cycloartenol, amyrin, lupeol, and isomultiflorenol.


Pssm-ID: 273809 [Multi-domain]  Cd Length: 621  Bit Score: 44.35  E-value: 6.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76253908    98 TLSAIQILSLYDSvNAIDVDKV----VEYVKGLQQEDGSFAGdKWGEIDTRFSFCAVATLALLGKL--DVINVDKAVEFV 171
Cdd:TIGR01787 441 TARVIQALGAFGH-RADEIRNVleraLEYLRREQRADGSWFG-RWGVNYTYGTGFVLSALAAAGRTyrNCPEVQKACDWL 518

                          90
                  ....*....|.
gi 76253908   172 MSCMNFDGGFG 182
Cdd:TIGR01787 519 LSRQMPDGGWG 529
SQCY cd02889
Squalene cyclase (SQCY) domain; found in class II terpene cyclases that have an alpha 6 - ...
 116-182 8.89e-04

Squalene cyclase (SQCY) domain; found in class II terpene cyclases that have an alpha 6 - alpha 6 barrel fold. Squalene cyclase (SQCY) and 2,3-oxidosqualene cyclase (OSQCY) are integral membrane proteins that catalyze a cationic cyclization cascade converting linear triterpenes to fused ring compounds. Bacterial SQCY catalyzes the convertion of squalene to hopene or diplopterol. Eukaryotic OSQCY transforms the 2,3-epoxide of squalene to compounds such as, lanosterol (a metabolic precursor of cholesterol and steroid hormones) in mammals and fungi or, cycloartenol in plants. Deletion of a single glycine residue of Alicyclobacillus acidocaldarius SQCY alters its substrate specificity into that of eukaryotic OSQCY. Both enzymes have a second minor domain, which forms an alpha-alpha barrel that is inserted into the major domain. This group also contains SQCY-like archael sequences and some bacterial SQCY's which lack this minor domain.


Pssm-ID: 239219 [Multi-domain]  Cd Length: 348  Bit Score: 40.67  E-value: 8.89e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 76253908 116 VDKVVEYVKGLQQEDGSFAGdKWGeID----TRFSFCAvatLALLGKLDVIN-VDKAVEFVMSCMNFDGGFG 182
Cdd:cd02889 193 IRRAVKYLEREQEPDGSWYG-RWG-VCfiygTWFALEA---LAAAGEDENSPyVRKACDWLLSKQNPDGGWG 259
hopene_cyclase TIGR01507
squalene-hopene cyclase; SHC is an essential prokaryotic gene in hopanoid (triterpenoid) ...
 116-182 1.62e-03

squalene-hopene cyclase; SHC is an essential prokaryotic gene in hopanoid (triterpenoid) biosynthesis. Squalene hopene cyclase, an integral membrane protein, directly cyclizes squalene into hopanoid products. [Fatty acid and phospholipid metabolism, Other]


Pssm-ID: 273661 [Multi-domain]  Cd Length: 635  Bit Score: 40.26  E-value: 1.62e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 76253908   116 VDKVVEYVKGLQQEDGSFAGdKWGeidTRFSFCAVATLALLGKLDVIN----VDKAVEFVMSCMNFDGGFG 182
Cdd:TIGR01507 473 IERAVEYLKREQEPDGSWFG-RWG---VNYLYGTGAVLSALKAVGIDTrepyIQKALAWLESHQNPDGGWG 539
PLN02993 PLN02993
lupeol synthase
 116-190 2.27e-03

lupeol synthase


Pssm-ID: 215537 [Multi-domain]  Cd Length: 763  Bit Score: 39.90  E-value: 2.27e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 76253908  116 VDKVVEYVKGLQQEDGSFAGDkWGEIDTRFSFCAVATLALLGKL--DVINVDKAVEFVMSCMNFDGGFGcrpgsESH 190
Cdd:PLN02993 592 IEKAVQFIESKQTPDGSWYGN-WGICFIYATWFALGGLAAAGKTynDCLAMRKGVHFLLTIQRDDGGWG-----ESY 662
DUF1828 pfam08861
Domain of unknown function DUF1828; This presumed domain is functionally uncharacterized.
 17-77 7.42e-03

Domain of unknown function DUF1828; This presumed domain is functionally uncharacterized.


Pssm-ID: 430268  Cd Length: 90  Bit Score: 35.26  E-value: 7.42e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 76253908    17 TLFLDKHADYIAAYGSKKDDYEYTLSEYlrmsgiywGLTVMDLMG---QLSRMNREEIIEFIKS 77
Cdd:pfam08861   1 TPFLDEDGDAIQIYVKKREGDRIRLTDD--------GYTLMHLSYsgcDLDSGKRKELLEAILS 56
SQCY_1 cd02892
Squalene cyclase (SQCY) domain subgroup 1; found in class II terpene cyclases that have an ...
 98-182 9.15e-03

Squalene cyclase (SQCY) domain subgroup 1; found in class II terpene cyclases that have an alpha 6 - alpha 6 barrel fold. Squalene cyclase (SQCY) and 2,3-oxidosqualene cyclase (OSQCY) are integral membrane proteins that catalyze a cationic cyclization cascade converting linear triterpenes to fused ring compounds. This group contains bacterial SQCY which catalyzes the convertion of squalene to hopene or diplopterol and eukaryotic OSQCY which transforms the 2,3-epoxide of squalene to compounds such as, lanosterol in mammals and fungi or, cycloartenol in plants. Deletion of a single glycine residue of Alicyclobacillus acidocaldarius SQCY alters its substrate specificity into that of eukaryotic OSQCY. Both enzymes have a second minor domain, which forms an alpha-alpha barrel that is inserted into the major domain.


Pssm-ID: 239222 [Multi-domain]  Cd Length: 634  Bit Score: 37.95  E-value: 9.15e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76253908  98 TLSAIQILSLY---------DSVNAIDvdKVVEYVKGLQQEDGSFAGdKWGeidTRFSFcavATLALLGKLDVINVD--- 165
Cdd:cd02892 453 TGSVLEALGLFgklypghrrEIDPAIR--RAVKYLLREQEPDGSWYG-RWG---VCYIY---GTWFALEALAAAGEDyen 523

                        90       100
                ....*....|....*....|..
gi 76253908 166 -----KAVEFVMSCMNFDGGFG 182
Cdd:cd02892 524 spyirKACDFLLSKQNPDGGWG 545
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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